ID   PTCA_LACLM              Reviewed;         116 AA.
AC   A2RIE7;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=PTS system galactose-specific EIIA component {ECO:0000305};
GN   Name=ptcA {ECO:0000303|PubMed:30123211};
GN   OrderedLocusNames=llmg_0438 {ECO:0000312|EMBL:CAL97042.1};
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RC   STRAIN=MG1363;
RX   PubMed=30123211; DOI=10.3389/fmicb.2018.01803;
RA   Solopova A., Bachmann H., Teusink B., Kok J., Kuipers O.P.;
RT   "Further elucidation of galactose utilization in Lactococcus lactis
RT   MG1363.";
RL   Front. Microbiol. 9:1803-1803(2018).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane (By
CC       similarity). Involved in galactose transport with PtcB and Lmg_0963
CC       (PubMed:30123211). {ECO:0000250|UniProtKB:P69791,
CC       ECO:0000269|PubMed:30123211}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P23532};
CC       Note=Binds 1 Mg(2+) ion per trimer. {ECO:0000250|UniProtKB:P23532};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P23532}.
CC   -!- INDUCTION: Induced by growth on galactose.
CC       {ECO:0000269|PubMed:30123211}.
CC   -!- DOMAIN: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00418}.
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DR   EMBL; AM406671; CAL97042.1; -; Genomic_DNA.
DR   RefSeq; WP_011675489.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; A2RIE7; -.
DR   SMR; A2RIE7; -.
DR   STRING; 416870.llmg_0438; -.
DR   EnsemblBacteria; CAL97042; CAL97042; llmg_0438.
DR   GeneID; 61108738; -.
DR   KEGG; llm:llmg_0438; -.
DR   eggNOG; COG1447; Bacteria.
DR   HOGENOM; CLU_152490_0_0_9; -.
DR   OMA; MEQSRMA; -.
DR   PhylomeDB; A2RIE7; -.
DR   BioCyc; LLAC416870:LLMG_RS02230-MON; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00215; PTS_IIA_lac; 1.
DR   InterPro; IPR003188; PTS_IIA_lac/cel.
DR   InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR   PANTHER; PTHR34382; PTHR34382; 1.
DR   Pfam; PF02255; PTS_IIA; 1.
DR   PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR   SUPFAM; SSF46973; SSF46973; 1.
DR   PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE   2: Evidence at transcript level;
KW   Magnesium; Metal-binding; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..116
FT                   /note="PTS system galactose-specific EIIA component"
FT                   /id="PRO_0000446881"
FT   DOMAIN          11..109
FT                   /note="PTS EIIA type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT   ACT_SITE        85
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P23532"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared between all trimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P23532"
FT   MOD_RES         85
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
SQ   SEQUENCE   116 AA;  12886 MW;  EA96BEFFA582D712 CRC64;
     MTDKYENPTS DDYMGVVMGI IMSGGNAKGL AFQAIQQAKD GKFAEAESSL NEASEQLREA
     HDVQTDLLTR LAQGEKIGWN LYMVHAQDHL MNAITFKDLA VEVVGQERRL QALENK